Intrinsically unstructured proteins.

TitleIntrinsically unstructured proteins.
Publication TypeJournal Article
Year of Publication2002
AuthorsTompa, P.
JournalTrends Biochem Sci
Date Published2002 Oct
KeywordsAmino Acid Sequence, Amino Acids, Entropy, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Protein Binding, Protein Conformation, Protein Denaturation, Protein Folding, Proteins, Static Electricity, Structure-Activity Relationship

The recent suggestion that the classical structure-function paradigm should be extended to proteins and protein domains whose native and functional state is intrinsically unstructured has received a great deal of support. There is ample evidence that the unstructured state, common to all living organisms, is essential for basic cellular functions; thus it deserves to be recognized as a separate functional and structural category within the protein kingdom. In this review, recent findings are surveyed to illustrate that this novel but rapidly advancing field has reached a point where these proteins can be comprehensively classified on the basis of structure and function.

Alternate JournalTrends Biochem. Sci.
PubMed ID12368089